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Database: UniProt
Entry: CLPX_MOUSE
LinkDB: CLPX_MOUSE
Original site: CLPX_MOUSE 
ID   CLPX_MOUSE              Reviewed;         634 AA.
AC   Q9JHS4; E9QLZ8; Q9WVD1;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 165.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial;
DE   Flags: Precursor;
GN   Name=Clpx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=11003706; DOI=10.1007/s003350010173;
RA   Corydon T.J., Wilsbech M., Jespersgaard C., Andresen B.S., Borglum A.D.,
RA   Pedersen S., Bolund L., Gregersen N., Bross P.;
RT   "Human and mouse mitochondrial orthologs of bacterial ClpX.";
RL   Mamm. Genome 11:899-905(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LYS-300.
RC   STRAIN=BALB/cJ;
RX   PubMed=10347188; DOI=10.1074/jbc.274.23.16311;
RA   Santagata S., Bhattacharyya D., Wang F.H., Singha N., Hodtsev A.,
RA   Spanopoulou E.;
RT   "Molecular cloning and characterization of a mouse homolog of bacterial
RT   ClpX, a novel mammalian class II member of the Hsp100/Clp chaperone
RT   family.";
RL   J. Biol. Chem. 274:16311-16319(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=22710082; DOI=10.1016/j.jsb.2012.06.001;
RA   Lowth B.R., Kirstein-Miles J., Saiyed T., Broetz-Oesterhelt H.,
RA   Morimoto R.I., Truscott K.N., Dougan D.A.;
RT   "Substrate recognition and processing by a Walker B mutant of the human
RT   mitochondrial AAA+ protein CLPX.";
RL   J. Struct. Biol. 179:193-201(2012).
CC   -!- FUNCTION: ATP-dependent specificity component of the Clp protease
CC       complex. Hydrolyzes ATP. Targets specific substrates for degradation by
CC       the Clp complex. Can perform chaperone functions in the absence of
CC       CLPP. Enhances the DNA-binding activity of TFAM and is required for
CC       maintaining a normal mitochondrial nucleoid structure
CC       (PubMed:10347188). ATP-dependent unfoldase that stimulates the
CC       incorporation of the pyridoxal phosphate cofactor into 5-
CC       aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA)
CC       synthesis, the first step in heme biosynthesis. Important for efficient
CC       erythropoiesis through up-regulation of heme biosynthesis (By
CC       similarity). {ECO:0000250|UniProtKB:O76031,
CC       ECO:0000269|PubMed:10347188}.
CC   -!- SUBUNIT: Homohexamer that forms a ring structure; this hexamerization
CC       requires ATP binding. Component of the Clp complex formed by the
CC       assembly of two CLPP heptameric rings with two CLPX hexameric rings,
CC       giving rise to a symmetrical structure with two central CLPP rings
CC       flanked by a CLPX ring at either end of the complex (PubMed:22710082).
CC       Interacts with TFAM (By similarity). {ECO:0000250|UniProtKB:O76031,
CC       ECO:0000269|PubMed:22710082}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22710082}.
CC       Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC       {ECO:0000269|PubMed:22710082}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01250}.
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DR   EMBL; AJ276991; CAC01232.1; -; mRNA.
DR   EMBL; AF134983; AAD42187.1; -; mRNA.
DR   EMBL; AC110235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS23288.1; -.
DR   RefSeq; NP_035932.2; NM_011802.3.
DR   AlphaFoldDB; Q9JHS4; -.
DR   SMR; Q9JHS4; -.
DR   BioGRID; 234776; 7.
DR   STRING; 10090.ENSMUSP00000015501; -.
DR   iPTMnet; Q9JHS4; -.
DR   PhosphoSitePlus; Q9JHS4; -.
DR   SwissPalm; Q9JHS4; -.
DR   EPD; Q9JHS4; -.
DR   jPOST; Q9JHS4; -.
DR   MaxQB; Q9JHS4; -.
DR   PaxDb; 10090-ENSMUSP00000015501; -.
DR   PeptideAtlas; Q9JHS4; -.
DR   ProteomicsDB; 285494; -.
DR   Pumba; Q9JHS4; -.
DR   Antibodypedia; 51984; 116 antibodies from 26 providers.
DR   DNASU; 270166; -.
DR   Ensembl; ENSMUST00000015501.11; ENSMUSP00000015501.5; ENSMUSG00000015357.11.
DR   GeneID; 270166; -.
DR   KEGG; mmu:270166; -.
DR   UCSC; uc009qdb.2; mouse.
DR   AGR; MGI:1346017; -.
DR   CTD; 10845; -.
DR   MGI; MGI:1346017; Clpx.
DR   VEuPathDB; HostDB:ENSMUSG00000015357; -.
DR   eggNOG; KOG0745; Eukaryota.
DR   GeneTree; ENSGT00390000017625; -.
DR   InParanoid; Q9JHS4; -.
DR   OMA; HRSDFTN; -.
DR   OrthoDB; 452393at2759; -.
DR   PhylomeDB; Q9JHS4; -.
DR   TreeFam; TF312884; -.
DR   BioGRID-ORCS; 270166; 11 hits in 77 CRISPR screens.
DR   ChiTaRS; Clpx; mouse.
DR   PRO; PR:Q9JHS4; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JHS4; Protein.
DR   Bgee; ENSMUSG00000015357; Expressed in spermatid and 244 other cell types or tissues.
DR   ExpressionAtlas; Q9JHS4; baseline and differential.
DR   Genevisible; Q9JHS4; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0009368; C:endopeptidase Clp complex; ISS:UniProtKB.
DR   GO; GO:0009841; C:mitochondrial endopeptidase Clp complex; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:Ensembl.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0016504; F:peptidase activator activity; ISO:MGI.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:UniProtKB.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   NCBIfam; TIGR00382; clpX; 1.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Metal-binding; Mitochondrion;
KW   Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..634
FT                   /note="ATP-dependent Clp protease ATP-binding subunit clpX-
FT                   like, mitochondrial"
FT                   /id="PRO_0000005519"
FT   DOMAIN          94..147
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   REGION          69..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT   BINDING         295..302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   MOD_RES         438
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O76031"
FT   MOD_RES         618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76031"
FT   MUTAGEN         300
FT                   /note="K->A: Loss of ATP hydrolysis."
FT                   /evidence="ECO:0000269|PubMed:10347188"
FT   CONFLICT        37
FT                   /note="V -> M (in Ref. 2; AAD42187)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="G -> A (in Ref. 2; AAD42187)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        457..458
FT                   /note="Missing (in Ref. 2; AAD42187)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="A -> R (in Ref. 1; CAC01232)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="A -> R (in Ref. 2; AAD42187)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   634 AA;  69229 MW;  E6AF4326113B7072 CRC64;
     MSSCGACTCG AAAARLLTTS LTSAQRGISC GRIHVPVLGR LGTTLDAQAL RRAPLRTFSE
     TPAYFASKDG ANKDGSGDGN KKSVTEGSSK KSGSGNSGKG GNQLRCPKCG DLCTHVETFV
     SSTRFVKCEK CHHFFVVLSE ADSKKSIIKE PESAAEAVKL AFQQKPPPPP KKIYNYLDKY
     VVGQSFAKKV LSVAVYNHYK RIYNNIPANL RQQAEAEKQT SLTPRELEIR RREDEYRFTK
     LLQIAGISPH GNALGASMQQ QVNQQMPQEK RGGEVLDSSQ DDIKLEKSNI LLLGPTGSGK
     TLLAQTLAKC LDVPFAICDC TTLTQAGYVG EDIESVIAKL LQDANYNVEK AQQGIVFLDE
     VDKIGSVPGI HQLRDVGGEG VQQGLLKLLE GTIVNVPEKN SRKLRGETVQ VDTTNVLFVA
     SGAFNGLDRI ISRRKNEKYL GFGTPSNLGK GRRAAAAADL ANRSGESNTH QDIEEKDRLL
     RHVEARDLIE FGMIPEFVGR LPVVVPLHSL DEKTLVQILT EPRNAVIPQY QALFSMDKCE
     LNVTEDALKA IARLALERKT GARGLRSIME KLLLEPMFEV PNSDIVCVEV DKEVVEGKKE
     PGYIRAPSKE SSEEEYDSGV EEDGWPRQAD AANS
//
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